Chaperone action of a cofactor in protein folding.

ABSTRACT: Previously, we have reported that ATP accelerates the folding and unfolding of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is a glycolytic enzyme utilizing NAD⁺ as a cofactor. Because ATP and NAD⁺ share the ADP moiety, we hypothesized that NAD⁺ also accelerates the folding of GAPDH and that the common structural motif between ATP and NAD⁺ is responsible for the chaperone activity. After confirming that NAD⁺ indeed accelerates the folding of GAPDH, we examined the chaperone activity of the structural fragments of NAD⁺ (ADP, AMP, adenosine, and nicotinamide monophosphate). Our finding showed that ADP and AMP significantly speed up the folding of GAPDH, while adenosine and nicotinamide monophosphate

SUBMITTER: Chen C 

PROVIDER: S-EPMC7314391 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature